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HEADER HYDROLASE 01-AUG-24 9IZT
TITLE CRYSTAL STRUCTURE OF A PU HYDROLYSIS ENZYME AES72 FROM COMAMONAS
TITLE 2 ACIDOVORANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL ESTERASE/LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: SEQUENCE REFERENCE FOR DELFTIA ACIDOVORANS (80866) IS
COMPND 6 NOT AVAILABLE IN UNIPROT AT THE TIME OF BIOCURATION. CURRENT SEQUENCE
COMPND 7 REFERENCE IS FROM UNIPROT ID A0A1I2L9V0.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DELFTIA ACIDOVORANS;
SOURCE 3 ORGANISM_TAXID: 80866;
SOURCE 4 GENE: SAMN04488025_10455;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS PU, DEGRADATION, ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HAN,Z.S.LI,J.W.LIU,W.D.LIU,W.L.DONG
REVDAT 1 04-FEB-26 9IZT 0
JRNL AUTH X.HAN,Z.S.LI,J.W.LIU,W.D.LIU,W.L.DONG
JRNL TITL CRYSTAL STRUCTURE OF A PU HYDROLYSIS ENZYME AES72 FROM
JRNL TITL 2 COMAMONAS ACIDOVORANS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.21_5207: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 48950
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2465
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.6400 - 3.8800 0.96 4598 245 0.1479 0.1916
REMARK 3 2 3.8800 - 3.0800 0.99 4661 254 0.1563 0.1764
REMARK 3 3 3.0800 - 2.6900 1.00 4698 252 0.1772 0.2218
REMARK 3 4 2.6900 - 2.4400 1.00 4692 246 0.1762 0.2235
REMARK 3 5 2.4400 - 2.2700 1.00 4676 247 0.1716 0.2201
REMARK 3 6 2.2700 - 2.1300 1.00 4676 256 0.1769 0.2280
REMARK 3 7 2.1300 - 2.0300 1.00 4690 224 0.1831 0.2393
REMARK 3 8 2.0300 - 1.9400 1.00 4650 264 0.1963 0.2392
REMARK 3 9 1.9400 - 1.8600 0.99 4657 237 0.2308 0.2610
REMARK 3 10 1.8600 - 1.8000 0.97 4487 240 0.2350 0.2869
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 4686
REMARK 3 ANGLE : 1.699 6372
REMARK 3 CHIRALITY : 0.067 702
REMARK 3 PLANARITY : 0.015 844
REMARK 3 DIHEDRAL : 6.160 646
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9IZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 07-AUG-24.
REMARK 100 THE DEPOSITION ID IS D_1300050047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-X
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54056
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU HYPIX-ARC 150
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48962
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M TRI
REMARK 280 -SODIUM CITRATE DIHYDRATE, 30% PEG4000, PH 5.6, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 26.19882
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.56050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 49.25715
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 26.19882
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.56050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 49.25715
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 381 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 MET B 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 7 CG CD OE1 OE2
REMARK 470 ARG A 10 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 11 CG CD OE1 NE2
REMARK 470 ARG A 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 18 CG CD OE1 OE2
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 GLU A 28 CG CD OE1 OE2
REMARK 470 ASP A 66 CG OD1 OD2
REMARK 470 ARG A 71 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 200 CG CD OE1 OE2
REMARK 470 LYS A 201 CG CD CE NZ
REMARK 470 HIS A 203 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 204 CG CD1 CD2
REMARK 470 LYS A 207 CG CD CE NZ
REMARK 470 GLU A 252 CG CD OE1 OE2
REMARK 470 GLU B 7 CG CD OE1 OE2
REMARK 470 GLN B 11 CG CD OE1 NE2
REMARK 470 GLU B 15 CG CD OE1 OE2
REMARK 470 GLN B 16 CG CD OE1 NE2
REMARK 470 GLU B 18 CG CD OE1 OE2
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 LYS B 22 CG CD CE NZ
REMARK 470 ASP B 66 CG OD1 OD2
REMARK 470 ARG B 68 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 71 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 200 CG CD OE1 OE2
REMARK 470 LYS B 201 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O SER B 45 O HOH B 301 2.17
REMARK 500 OE1 GLU A 122 O HOH A 301 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 41 76.17 -113.34
REMARK 500 SER A 147 -127.45 57.29
REMARK 500 TRP A 196 -61.89 -124.08
REMARK 500 SER B 41 75.47 -109.44
REMARK 500 SER B 147 -127.31 56.25
REMARK 500 TRP B 196 -64.01 -123.04
REMARK 500 GLU B 268 -0.51 74.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 584 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH B 632 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 633 DISTANCE = 6.24 ANGSTROMS
DBREF1 9IZT A 1 297 UNP A0A1I2L9V0_9BACL
DBREF2 9IZT A A0A1I2L9V0 1 297
DBREF1 9IZT B 1 297 UNP A0A1I2L9V0_9BACL
DBREF2 9IZT B A0A1I2L9V0 1 297
SEQADV 9IZT LEU A 69 UNP A0A1I2L9V LYS 69 CONFLICT
SEQADV 9IZT ASN A 228 UNP A0A1I2L9V ARG 228 CONFLICT
SEQADV 9IZT LEU B 69 UNP A0A1I2L9V LYS 69 CONFLICT
SEQADV 9IZT ASN B 228 UNP A0A1I2L9V ARG 228 CONFLICT
SEQRES 1 A 297 MET ALA SER PRO GLN SER GLU ALA ILE ARG GLN MET LEU
SEQRES 2 A 297 ARG GLU GLN LYS GLU ALA ALA LYS LYS GLY ALA PRO SER
SEQRES 3 A 297 ILE GLU GLU GLN ARG ARG GLN LEU ASP TYR LEU GLY GLY
SEQRES 4 A 297 PHE SER PRO LEU GLU SER ASP VAL THR VAL GLU LYS THR
SEQRES 5 A 297 ARG ILE ALA GLY VAL PRO GLY GLU TRP ILE SER THR PRO
SEQRES 6 A 297 ASP ALA ARG LEU ASP ARG VAL LEU PHE TYR LEU HIS GLY
SEQRES 7 A 297 GLY ALA TYR CYS PHE GLY SER CYS ASP SER HIS ARG GLY
SEQRES 8 A 297 LEU VAL SER ARG LEU ALA ARG ALA CYS GLY SER ARG ALA
SEQRES 9 A 297 LEU LEU ILE GLU TYR ARG LEU ALA PRO GLU HIS PRO PHE
SEQRES 10 A 297 PRO ALA ALA LEU GLU ASP SER THR ALA ALA TYR ARG GLU
SEQRES 11 A 297 LEU ILE ARG SER GLY VAL ARG PRO GLU ASN LEU VAL ILE
SEQRES 12 A 297 ALA GLY ASP SER ALA GLY GLY GLY LEU THR MET ALA THR
SEQRES 13 A 297 LEU LEU THR LEU ARG ASP GLU GLY ASP PRO LEU PRO SER
SEQRES 14 A 297 ALA ALA VAL LEU LEU SER PRO TRP THR ASP LEU GLU GLY
SEQRES 15 A 297 THR GLY GLU SER MET LYS THR LYS ALA ASP VAL GLU PRO
SEQRES 16 A 297 TRP LEU ASP PRO GLU LYS SER HIS LEU LEU ALA LYS LEU
SEQRES 17 A 297 TYR LEU GLY ASP LEU ASP PRO ARG HIS PRO LEU VAL SER
SEQRES 18 A 297 PRO ILE HIS ALA ASP LEU ASN ASN LEU PRO PRO LEU LEU
SEQRES 19 A 297 VAL HIS VAL GLY SER ASP GLU CYS LEU LEU ASP ASP SER
SEQRES 20 A 297 VAL ARG LEU VAL GLU ARG ALA LYS SER ALA GLY VAL GLU
SEQRES 21 A 297 THR GLU PHE LYS ILE TRP ASP GLU MET TRP HIS VAL PHE
SEQRES 22 A 297 HIS GLY PHE PRO ILE PRO GLU ALA GLN GLN ALA ILE GLU
SEQRES 23 A 297 GLU ILE GLY ALA PHE VAL ARG ALA ARG LEU PRO
SEQRES 1 B 297 MET ALA SER PRO GLN SER GLU ALA ILE ARG GLN MET LEU
SEQRES 2 B 297 ARG GLU GLN LYS GLU ALA ALA LYS LYS GLY ALA PRO SER
SEQRES 3 B 297 ILE GLU GLU GLN ARG ARG GLN LEU ASP TYR LEU GLY GLY
SEQRES 4 B 297 PHE SER PRO LEU GLU SER ASP VAL THR VAL GLU LYS THR
SEQRES 5 B 297 ARG ILE ALA GLY VAL PRO GLY GLU TRP ILE SER THR PRO
SEQRES 6 B 297 ASP ALA ARG LEU ASP ARG VAL LEU PHE TYR LEU HIS GLY
SEQRES 7 B 297 GLY ALA TYR CYS PHE GLY SER CYS ASP SER HIS ARG GLY
SEQRES 8 B 297 LEU VAL SER ARG LEU ALA ARG ALA CYS GLY SER ARG ALA
SEQRES 9 B 297 LEU LEU ILE GLU TYR ARG LEU ALA PRO GLU HIS PRO PHE
SEQRES 10 B 297 PRO ALA ALA LEU GLU ASP SER THR ALA ALA TYR ARG GLU
SEQRES 11 B 297 LEU ILE ARG SER GLY VAL ARG PRO GLU ASN LEU VAL ILE
SEQRES 12 B 297 ALA GLY ASP SER ALA GLY GLY GLY LEU THR MET ALA THR
SEQRES 13 B 297 LEU LEU THR LEU ARG ASP GLU GLY ASP PRO LEU PRO SER
SEQRES 14 B 297 ALA ALA VAL LEU LEU SER PRO TRP THR ASP LEU GLU GLY
SEQRES 15 B 297 THR GLY GLU SER MET LYS THR LYS ALA ASP VAL GLU PRO
SEQRES 16 B 297 TRP LEU ASP PRO GLU LYS SER HIS LEU LEU ALA LYS LEU
SEQRES 17 B 297 TYR LEU GLY ASP LEU ASP PRO ARG HIS PRO LEU VAL SER
SEQRES 18 B 297 PRO ILE HIS ALA ASP LEU ASN ASN LEU PRO PRO LEU LEU
SEQRES 19 B 297 VAL HIS VAL GLY SER ASP GLU CYS LEU LEU ASP ASP SER
SEQRES 20 B 297 VAL ARG LEU VAL GLU ARG ALA LYS SER ALA GLY VAL GLU
SEQRES 21 B 297 THR GLU PHE LYS ILE TRP ASP GLU MET TRP HIS VAL PHE
SEQRES 22 B 297 HIS GLY PHE PRO ILE PRO GLU ALA GLN GLN ALA ILE GLU
SEQRES 23 B 297 GLU ILE GLY ALA PHE VAL ARG ALA ARG LEU PRO
FORMUL 3 HOH *617(H2 O)
HELIX 1 AA1 SER A 3 GLY A 23 1 21
HELIX 2 AA2 SER A 26 GLY A 39 1 14
HELIX 3 AA3 SER A 85 GLY A 101 1 17
HELIX 4 AA4 PRO A 118 SER A 134 1 17
HELIX 5 AA5 ARG A 137 GLU A 139 5 3
HELIX 6 AA6 SER A 147 GLY A 164 1 18
HELIX 7 AA7 GLU A 185 LYS A 190 1 6
HELIX 8 AA8 ASP A 198 GLY A 211 1 14
HELIX 9 AA9 SER A 221 ALA A 225 5 5
HELIX 10 AB1 LEU A 243 ALA A 257 1 15
HELIX 11 AB2 VAL A 272 PHE A 276 5 5
HELIX 12 AB3 ILE A 278 LEU A 296 1 19
HELIX 13 AB4 SER B 3 GLY B 23 1 21
HELIX 14 AB5 SER B 26 GLY B 39 1 14
HELIX 15 AB6 SER B 85 GLY B 101 1 17
HELIX 16 AB7 PRO B 118 SER B 134 1 17
HELIX 17 AB8 ARG B 137 GLU B 139 5 3
HELIX 18 AB9 SER B 147 GLU B 163 1 17
HELIX 19 AC1 GLU B 185 LYS B 190 1 6
HELIX 20 AC2 ASP B 198 GLY B 211 1 14
HELIX 21 AC3 SER B 221 ALA B 225 5 5
HELIX 22 AC4 LEU B 243 ALA B 257 1 15
HELIX 23 AC5 VAL B 272 PHE B 276 5 5
HELIX 24 AC6 ILE B 278 LEU B 296 1 19
SHEET 1 AA1 8 THR A 48 ILE A 54 0
SHEET 2 AA1 8 VAL A 57 SER A 63 -1 O SER A 63 N THR A 48
SHEET 3 AA1 8 SER A 102 ILE A 107 -1 O ALA A 104 N ILE A 62
SHEET 4 AA1 8 ARG A 68 LEU A 76 1 N LEU A 73 O ARG A 103
SHEET 5 AA1 8 LEU A 141 ASP A 146 1 O ALA A 144 N LEU A 76
SHEET 6 AA1 8 ALA A 170 LEU A 174 1 O LEU A 174 N GLY A 145
SHEET 7 AA1 8 LEU A 233 GLY A 238 1 O LEU A 234 N LEU A 173
SHEET 8 AA1 8 THR A 261 TRP A 266 1 O TRP A 266 N VAL A 237
SHEET 1 AA2 8 THR B 48 ILE B 54 0
SHEET 2 AA2 8 VAL B 57 SER B 63 -1 O SER B 63 N THR B 48
SHEET 3 AA2 8 SER B 102 ILE B 107 -1 O ALA B 104 N ILE B 62
SHEET 4 AA2 8 ARG B 68 LEU B 76 1 N LEU B 73 O ARG B 103
SHEET 5 AA2 8 LEU B 141 ASP B 146 1 O ALA B 144 N LEU B 76
SHEET 6 AA2 8 ALA B 170 LEU B 174 1 O LEU B 174 N GLY B 145
SHEET 7 AA2 8 LEU B 233 GLY B 238 1 O LEU B 234 N LEU B 173
SHEET 8 AA2 8 THR B 261 TRP B 266 1 O TRP B 266 N VAL B 237
CISPEP 1 ALA A 112 PRO A 113 0 3.45
CISPEP 2 PHE A 117 PRO A 118 0 8.58
CISPEP 3 ALA B 112 PRO B 113 0 2.66
CISPEP 4 PHE B 117 PRO B 118 0 7.70
CRYST1 77.161 71.121 101.579 90.00 104.11 90.00 I 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012960 0.000000 0.003257 0.00000
SCALE2 0.000000 0.014060 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010151 0.00000
TER 2221 PRO A 297
TER 4460 PRO B 297
MASTER 303 0 0 24 16 0 0 6 5075 2 0 46
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